Weitere Antikörper gegen USP8 Interaktionspartner

Human Ubiquitin Specific Peptidase 8 (USP8) Interaktionspartner

Deubiquitination of EPG5 by USP8 guards the autophagic flux in embryonic stem cells (ESCs) to maintain their stemness. This work uncovers a novel crosstalk pathway between ubiquitination and autophagy through USP8-EPG5 interaction to regulate the stemness of ESCs.

High expression of USP8 was correlated with advanced tumor stage and high recurrence risk. Moreover, USP8 was identified as a novel independent prognostic factor for CSCC patients.

In summary, we show that, contrary to the pituitary ACTH-secreting tumors, the USP8 hotspot sequence on exon 14 is not mutated in tumors causing ectopic ACTH secretion syndrome (EAS). Although USP8 is expressed in all EAS tumors examined, our in vitro data indicate that it is not involved in the regulation of ectopic proopiomelanocortin transcription.

Overexpression of USP8 in lung adenocarcinoma is an early event during the course of tumor progression, and is related to EGFR expression.

Somatic mutations in USP8 are common in Nelson's tumors, and are associated with less favorable outcome after surgery.

Data indicate that USP8 functions as a novel deubiquitylase of FLIPL and inhibits extrinsic apoptosis by stabilizing FLIPL.

Somatic USP8 gene mutations are a common cause of pediatric Cushing disease due to pituitary adenoma.

findings demonstrate that USP8 plays a key role in the trafficking and degradation of BACE1 by deubiquitinating lysine 501.

USP8 regulates VEGFR2 trafficking, signaling and proteolysis.

Ubpy loss of function results in the accumulation of autophagosomes due to a blockade of the autophagy flux.

Results show that in addition to the scaffolding function in complex formation, BRUCE has an E3 ligase function to promote BRIT1 deubiquitination by USP8 leading to accumulation of BRIT1 at DNA double-strand break.

Deubiquitination of EPG5 by USP8 guards the autophagic flux in embryonic stem cells (ESCs) to maintain their stemness. This work uncovers a novel crosstalk pathway between ubiquitination and autophagy through USP8-EPG5 interaction to regulate the stemness of ESCs.

UBPy-sorted cargo to acrosome biogenesis and effects of its derailment in a mouse model of globozoospermia, the infertile Vps54 (L967Q) mutant, are reported.

the membrane receptor MET, described herein for the first time in spermatids, is a USP8/UBPy-target substrate is delivered to the acrosome.

in neuronal cells USP8 could be involved in endosomal trafficking, retrograde transport and synaptic plasticity. In disorders leading to neurodegeneration USP8 is upregulated and could influence the neuron-oligodendrocyte interactions.

The spatio-temporal expression of mUBPy suggests that the enzyme may be involved in neuroregulatory processes during embryogenesis.

a role for the USP8.STAM complex as a protective mechanism regulating early endosomal sorting of EGFR between pathways destined for lysosomal degradation and recycling.

USP8 was able to interact with spermatid endosomal-sorting complex required for transport-0 and microtubule structures; USP8 can directly link, via its MIT domain, the labeled vesicles/developing acrosome to microtubules.

in wobbler testis expression of mouse ubiquitin-specific processing protease (mUBPy)is up-regulated, while a differential sorting of the protein characterizes wobbler spermatids where acrosome formation is impaired

deubiquitinating enzyme specifically expressed in testis, associates with the acrosome and centrosome in mouse germ cells

Results indicate that Nrdp1 is a specific target for the USP8 deubiquitinating enzyme and are consistent with a model where USP8 augments Nrdp1 activity by mediating its stabilization.

We conclude that UBPY negatively regulates the rate of EGFR down-regulation by deubiquitinating EGFR on endosomes.

UBPY-mediated EGFR de-ubiquitination promotes EGFR degradation

UBPy may play a key role during mouse fertilization as a novel centrosomal component.

These results unveil a central and nonredundant role of UBPy in growth regulation, endosomal sorting, and the control of receptor tyrosine kinases in vivo.

UBPY is catalytically inhibited in a phosphorylation-dependent manner by 14-3-3s during the interphase, and this regulation is cancelled in the M phase.

Moderate expression of mouse UBPy was found in the amygdaloid complex, supraoptic nucleus, arcuate and ventromedial nuclei of hypothalamus, lateral hypothalamic area and lateral and reticular part of the substantia nigra.

USP8 Antigen-Profil

Protein Überblick

Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1.